Evidence map›Paper›PMID 20826808›Full record

ArticleThe Journal of biological chemistry2010

A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring.

Darren E Casteel, Eric V Smith-Nguyen, Banumathi Sankaran, Sung H Roh, Renate B Pilz, Choel Kim

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 35 citations in OpenAlex.

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  11. A bioinformatic and computational study of myosin phosphatase subunit diversity.American journal of physiology. Regulatory, integrative and comparative physiology · 2014
    Article
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  13. Review
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  17. cGMP becomes a drug target.Naunyn-Schmiedeberg's archives of pharmacology · 2012
    Review
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Darren E CasteelFrom the Department of Medicine and Cancer Center, San Diego, La Jolla, California 92093.
Eric V Smith-NguyenDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093.
Banumathi SankaranBerkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
Sung H RohDepartment of Pharmacology, Baylor College of Medicine, Houston, Texas 77030.
Renate B PilzFrom the Department of Medicine and Cancer Center, San Diego, La Jolla, California 92093.
Choel KimDepartment of Pharmacology, Baylor College of Medicine, Houston, Texas 77030. Electronic address: ckim@bcm.edu.
University of California San Diego · USBaylor College of Medicine · USLawrence Berkeley National Laboratory · US

Funding

REGULATION OF GENE EXPRESSION BY cGMP and PKG IN BONER01AR051300 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PILZ, RENATE B · 2004 to 2014
$3.1M
Targeting mechanisms of cGMP dependent protein kinases by peptide arrays and crysR01GM090161 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI KIM, CHOEL WOONG · 2010 to 2018
$2.9M
Study of mTOR Regulation by Rheb Using Deuterium Exchange Mass SpectrometryK22CA124517 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CASTEEL, DARREN E · 2007 to 2009
$423k
NCI NIH HHS K22 CA124517NCI NIH HHS K22-CA124517NIAMS NIH HHS R01 AR051300NIAMS NIH HHS R01-AR051300NIGMS NIH HHS R01 GM090161
6 · The paper itself

Abstract

Cyclic GMP-dependent protein kinase (PKG) is a key mediator of the nitric oxide/cGMP signaling pathway and plays a central role in regulating cardiovascular and neuronal functions. The N-terminal ∼50 amino acids of the kinase are required for homodimerization and association with isoform-specific PKG-anchoring proteins (GKAPs), which target the kinase to specific substrates. To understand the molecular details of PKG dimerization and gain insight into its association with GKAPs, we solved a crystal structure of the PKG Iβ dimerization/docking domain. Our structure provides molecular details of this unique leucine/isoleucine zipper, revealing specific hydrophobic and ionic interactions that mediate dimerization and demonstrating the topology of the GKAP interaction surface.

Indexed as

AnimalsCrystallography, X-RayCyclic GMP-Dependent Protein KinasesHumansIsoenzymesLeucine ZippersMiceMice, TransgenicProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryStructure-Activity RelationshipCyclic GMP-Dependent Protein KinasesIsoenzymes

Identifiers

PMID20826808
PMCPMC2963381
OpenAlexW2100594878

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.